Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H

Journal of Molecular Biology

Volumn 329, Issue 4, 2003, Pages 731-743

  Guzman Casado, Mercedes ^a   Parody Morreale, Antonio ^a   Robic, Srebrenka ^b   Marqusee, Susan ^b   Sanchez Ruiz, Jose M ^a  

^a UNIVERSITY OF GRANADA   (Spain)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Denatured state; Hydrophobic cluster; Thermophilic protein

Indexed keywords

ASPARTIC ACID; CARBOXYLIC ACID; GLUTAMINE; RIBONUCLEASE H;

ARTICLE; ELECTRICITY; ENZYME ANALYSIS; ENZYME DENATURATION; ESCHERICHIA COLI; HEAT; HYDROPHILICITY; HYDROPHOBICITY; NONHUMAN; OPTICAL ROTATION; PH; PREDICTION; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT; SURFACE PROPERTY; TEMPERATURE; THERMOPHILIC BACTERIUM; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS; THERMUS THERMOPHILUS;

EID: 0038392707     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00513-8     Document Type: Article

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